SNAREs and NSF in targeted membrane fusion

• Published in: Current opinion in cell biology Vol. 9; no. 4; pp. 505 - 512
• Main Authors: Hay, Jesse C, Scheller, Richard H
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.08.1997
• Subjects: Animals; Carrier Proteins - physiology; Endoplasmic Reticulum - physiology; Endosomes - physiology; Golgi Apparatus - physiology; Homeostasis; Intracellular Membranes - physiology; Lysosomes - physiology; Membrane Fusion; Membrane Proteins - physiology; Models, Biological; SNARE Proteins; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; Vacuoles - physiology; Vesicular Transport Proteins; NSF N-ethylmaleimide-sensitive factor; VAMP vesicle-associated membrane protein; SNAP-25 synaptosome-associated protein of 25 kDa; t-SNARE SNARE on target membrane; called Sec 18p in yeast; called Sec17p in yeast; TGN trans-Golgi network; ER endoplasmic reticulum; α-SNAP α-soluble NSF-attachment protein; GOS-28 Golgi-associated SNARE of 28 kDa; v-SNARE SNARE on vesicle; SNARE SNAP receptor
• ISSN: 0955-0674; 1879-0410
• DOI: 10.1016/S0955-0674(97)80026-9

A major current issue in vesicle trafficking is whether NSF ( N-ethylmaleimide-sensitive factor) and α-SNAP (α-soluble NSF attachment protein) are required prior to SNARE (SNAP receptor) complex formation to allow vesicle docking, or after docking at a step close to membrane fusion. Recent studies of yeast vacuolar fusion indicated that the requirement for ATP, NSF and α-SNAP could be completely satisfied prior to SNARE docking complex assembly; however, the universality of a predocking role for these factors remains to be established. The vacuolar fusion system has also been used to directly demonstrate a requirement for SNARE proteins on both fusing membranes, verifying a central postulate of current fusion models.